Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids into smaller pieces. It is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyzes proteins.[2][3] Trypsin is formed in the small intestine when its proenzyme form, the trypsinogen produced by the pancreas, is activated. Trypsin cuts peptide chains mainly at the carboxyl side of the amino acids lysine or arginine. It is used for numerous biotechnological processes. The process is commonly referred to as trypsinogen proteolysis or trypsinization, and proteins that have been digested/treated with trypsin are said to have been trypsinized.[4]
Trypsin was discovered in 1876 by Wilhelm Kühne.[5] Although many sources say that Kühne named trypsin from the Ancient Greek word for rubbing, 'tripsis', because the enzyme was first isolated by rubbing the pancreas with glass powder and alcohol, in fact Kühne named trypsin from the Ancient Greek word 'thrýpto' which means 'I break' or 'I break apart'.[6]
^PDB: 1UTN; Leiros HK, Brandsdal BO, Andersen OA, Os V, Leiros I, Helland R, et al. (April 2004). "Trypsin specificity as elucidated by LIE calculations, X-ray structures, and association constant measurements". Protein Science. 13 (4): 1056–70. doi:10.1110/ps.03498604. PMC 2280040. PMID 15044735.
^Rawlings ND, Barrett AJ (1994). "[2] Families of serine peptidases". Families of serine peptidases. Methods in Enzymology. Vol. 244. pp. 19–61. doi:10.1016/0076-6879(94)44004-2. ISBN 978-0-12-182145-6. PMC 7133253. PMID 7845208.
^The German physiologist Wilhelm Kühne (1837-1900) discovered trypsin in 1876. See: Kühne W (1877). "Über das Trypsin (Enzym des Pankreas)". Verhandlungen des Naturhistorisch-medicinischen Vereins zu Heidelberg. new series. 1 (3): 194–198 – via Google Books.
^Engelking LR (2015-01-01). "Chapter 7 - Protein Digestion". Textbook of Veterinary Physiological Chemistry (Third ed.). Boston: Academic Press. pp. 39–44. doi:10.1016/B978-0-12-391909-0.50007-4. ISBN 978-0-12-391909-0.
^Kühne W (March 6, 1876). "Ueber das Trypsin (Enzym des Pankreas)" [About trypsin (enzyme of the pancreas)]. In Naturhistorisch-medizinischen Verein (ed.). Verhandlungen des Naturhistorisch-medizinischen Vereins zu Heidelberg [Negotiations by the Natural History Medical Association in Heidelberg] (in German). Heidelberg, Germany: Carl Winter's Universitätsbuchhandlung (published 1877). pp. 194–8 – via Archive.org.
^Girolami GS (2024). "Origin and Likely Etymology of the Word 'Trypsin'". Bull. Hist. Chem. 49 (1): 59–60.
Trypsin is an enzyme in the first section of the small intestine that starts the digestion of protein molecules by cutting long chains of amino acids...
A trypsin inhibitor (TI) is a protein and a type of serine protease inhibitor (serpin) that reduces the biological activity of trypsin by controlling the...
Trypsin-1, also known as cationic trypsinogen, is a protein that in humans is encoded by the PRSS1 gene. Trypsin-1 is the main isoform of trypsinogen secreted...
into two broad categories based on their structure: chymotrypsin-like (trypsin-like) or subtilisin-like. The MEROPS protease classification system counts...
pancreatic trypsin inhibitor (BPTI), or basic trypsin inhibitor of bovine pancreas, which is an antifibrinolytic molecule that inhibits trypsin and related...
Trypsinogen (/ˌtrɪpˈsɪnədʒən, -ˌdʒɛn/) is the precursor form (or zymogen) of trypsin, a digestive enzyme. It is produced by the pancreas and found in pancreatic...
that first renders the body of the animal transparent by bathing it in trypsin, and then stains the bones and cartilage with various dyes, usually alizarin...
produced and has molecular weight of 25 - 40kDa. It acts as a urinary trypsin inhibitor (UTI). Highly purified ulinastatin has been clinically used for...
soybean trypsin inhibitor is a type of protein contained in legume seeds which functions as a protease inhibitor. Kunitz-type Soybean Trypsin Inhibitors...
serine, 2 (trypsin 2) is a protein that in humans is encoded by the PRSS2 gene. This gene encodes a trypsinogen, which is a member of the trypsin family of...
supervised by Richard L. Lyman, was titled The isolation and purification of a trypsin inhibitor from whole wheat flour. Shyamala conducted research in UC Berkeley's...
Trypsinization is the process of cell dissociation using trypsin, a proteolytic enzyme which breaks down proteins, to dissociate adherent cells from the...
clan). Each family may contain many hundreds of related proteases (e.g. trypsin, elastase, thrombin and streptogrisin within the S1 family). Currently...
One of the plant's defenses against some insect attacks is the cowpea trypsin inhibitor (CpTI). CpTI has been transgenically inserted into other crops...
proteins by the host MCP. Similarly, they inhibit trypsin by releasing the protein Ascaris Trypsin Inhibitor (pdb 1ATA). Ascaris has been present in humans...
assortment of peptides formed by the digestion of casein by the protease trypsin. Tryptone is commonly used in microbiology to produce lysogeny broth (LB)...
Lentils also have antinutrient factors, such as trypsin inhibitors and a relatively high phytate content. Trypsin is an enzyme involved in digestion, and phytates...
Wendell Meredith Stanley, who worked on the digestive enzymes pepsin (1930), trypsin and chymotrypsin. These three scientists were awarded the 1946 Nobel Prize...
that break down proteins begin with activation of trypsinogen to trypsin. The free trypsin then cleaves the rest of the trypsinogen, as well as chymotrypsinogen...
Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes...
Panniculitis is a group of diseases whose hallmark is inflammation of subcutaneous adipose tissue (the fatty layer under the skin – panniculus adiposus)...
proteases such as caspase, papain, bromelain or ficin. It does not inhibit trypsin or zymogens. TPCK is observed covalently bound in the active site of Caspase...
an energy and protein source as animal feed. Raw chickpeas have a lower trypsin and chymotrypsin inhibitor content than peas, common beans, and soybeans...
peptide, also known as pancreatic secretory trypsin inhibitor I (PSTI-I) or pancreatic secretory trypsin inhibitor 61 (PSTI-61), is a peptide that plays...
the catalytic triad of enzymes such as proteases like chymotrypsin and trypsin, where an acyl-enzyme intermediate is formed. An alternative mechanism...
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